Linked Life Data

8703027

Source:http://linkedlifedata.com/resource/pubmed/id/8703027

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pubmed-article:8703027pubmed:abstractTextThe phagocyte NADPH oxidase is activated during phagocytosis to produce superoxide, a precursor of microbicidal oxidants. The activation involves assembly of membrane-integrated cytochrome b558 comprising gp91(phox) and p22(phox), two specialized cytosolic proteins (p47(phox) and p67(phox)), each containing two Src homology 3 (SH3) domains, and the small G protein Rac. In the present study, we show that the N-terminal SH3 domain of p47(phox) binds to the C-terminal cytoplasmic tail of p22(phox) with high affinity (KD = 0.34 microM). The binding is specific to this domain among several SH3 domains including the C-terminal one of p47(phox) and the two of p67(phox) and requires the Pro156-containing proline-rich sequence but not other putative SH3 domain-binding sites of p22(phox). Replacement of Trp193 by Arg in the N-terminal SH3 domain completely abrogates the association with p22(phox). A mutant p47(phox) with this substitution is incapable of supporting superoxide production under cell-free activation conditions. These findings provide direct evidence that the interaction between the N-terminal SH3 domain of p47(phox) and the proline-rich region of p22(phox) is essential for activation of the NADPH oxidase.lld:pubmed
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pubmed-article:8703027pubmed:articleTitleAssembly and activation of the phagocyte NADPH oxidase. Specific interaction of the N-terminal Src homology 3 domain of p47phox with p22phox is required for activation of the NADPH oxidase.lld:pubmed
pubmed-article:8703027pubmed:affiliationDepartment of Biochemistry, Kyushu University School of Medicine, Fukuoka 812, Japan.lld:pubmed
pubmed-article:8703027pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8703027pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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